Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-2-18
pubmed:abstractText
We describe a novel Escherichia coli protein, DjlA, containing a highly conserved J-region motif, which is present in the DnaJ protein chaperone family and required for interaction with DnaK. Remarkably, DjlA is shown to be a membrane protein, localized to the inner membrane with the unusual Type III topology (N-out, C-in). Thus, DjlA appears to present an extremely short N-terminus to the periplasm and has a single transmembrane domain (TMD) and a large cytoplasmic domain containing the C-terminal J-region. Analysis of the TMD of DjlA and recently identified homologues in Coxiella burnetti and Haemophilus influenzae revealed a striking pattern of conserved glycines (or rarely alanine), with a four-residue spacing. This motif, predicted to form a spiral groove in the TMD, is more marked than a repeating glycine motif, implicated in the dimerization of TMDs of some eukaryotic proteins. This feature of DjlA could represent a promiscuous docking mechanism for interaction with a variety of membrane proteins. DjlA null mutants can be isolated but these appear rapidly to accumulate suppressors to correct envelope and growth defects. Moderate (10-fold) overproduction of DjlA suppresses a mutation in FtsZ but markedly perturbs cell division and cell-envelope growth in minimal medium. We propose that DjlA plays a role in the correct assembly, activity and/or maintenance of a number of membrane proteins, including two-component signal-transduction systems.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DnaJ protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FtsZ protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/HSP40 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/colanic acid
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1273-86
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8809778-Amino Acid Sequence, pubmed-meshheading:8809778-Animals, pubmed-meshheading:8809778-Antibodies, Bacterial, pubmed-meshheading:8809778-Bacterial Proteins, pubmed-meshheading:8809778-Cell Extracts, pubmed-meshheading:8809778-Cell Membrane, pubmed-meshheading:8809778-Culture Media, pubmed-meshheading:8809778-Cytoskeletal Proteins, pubmed-meshheading:8809778-Escherichia coli, pubmed-meshheading:8809778-Escherichia coli Proteins, pubmed-meshheading:8809778-HSP40 Heat-Shock Proteins, pubmed-meshheading:8809778-Heat-Shock Proteins, pubmed-meshheading:8809778-Membrane Proteins, pubmed-meshheading:8809778-Molecular Sequence Data, pubmed-meshheading:8809778-Mutation, pubmed-meshheading:8809778-Phenotype, pubmed-meshheading:8809778-Polysaccharides, pubmed-meshheading:8809778-Polysaccharides, Bacterial, pubmed-meshheading:8809778-Rabbits, pubmed-meshheading:8809778-Recombinant Fusion Proteins
pubmed:year
1996
pubmed:articleTitle
A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology.
pubmed:affiliation
Institut de Génétique et Microbiologie, URA 1354, Université Paris-Sud, Orsay, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't